P13, an integral membrane protein of Borrelia burgdorferi, is C-terminally processed and contains surface-exposed domains

To elucidate antigens present an the bacterial surface of Borrelia burgdorferi sensu late that may be involved in pathogenesis, we characterized a protein, P13, with an apparent molecular mass of 13 kDa. The protein was immunogenic and was expressed in large amounts during in vitro cultivation compared to other known antigens, An immunofluorescence assay, immunoelectron microscopy, and protease sensitivity assays indicated that P13 is surface exposed, The deduced sequence of the PW peptide revealed a possible signal peptidase type I cleavage site, and computer analysis predicted that P13 is an integral membrane protein with three transmembrane-spanning domains. Mass spectrometry in vitro translation, and N- and C-terminal amino acid sequencing analyses indicated that P13 was posttranslationally processed at both ends and modified by an unknown mechanism. Furthermore, p13 belongs to a gene family with five additional members in B. burgdorferi sensu stricto, The p13 gene is located on the linear chromosome of the bacterium, in contrast to five paralogous genes, which are located on extrachromosomal plasmids, The size of the p13 transcript was consistent with a manocistronic transcript. This new gene family may be involved in functions that are specific for this spirochete and its pathogenesis.